1pmu: Difference between revisions

Revision as of 20:51, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1pmu.png

Template:STRUCTURE 1pmu

The crystal structure of JNK3 in complex with a phenantroline inhibitorThe crystal structure of JNK3 in complex with a phenantroline inhibitor

Template:ABSTRACT PUBMED 12954329

About this StructureAbout this Structure

1PMU is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

The structure of JNK3 in complex with small molecule inhibitors: structural basis for potency and selectivity., Scapin G, Patel SB, Lisnock J, Becker JW, LoGrasso PV, Chem Biol. 2003 Aug;10(8):705-12. PMID:12954329

Page seeded by OCA on Mon Jul 28 20:51:04 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''The crystal structure of JNK3 in complex with a phenantroline inhibitor'''
+===The crystal structure of JNK3 in complex with a phenantroline inhibitor===
-==Overview==
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-The c-Jun terminal kinases (JNKs) are members of the mitogen-activated protein (MAP) kinase family and regulate signal transduction in response to environmental stress. Activation of JNK3, a neuronal-specific isoform, has been associated with neurological damage, and as such, JNK3 may represent an attractive target for the treatment of neurological disorders. The MAP kinases share between 50% and 80% sequence identity. In order to obtain efficacious and safe compounds, it is necessary to address the issues of potency and selectivity. We report here four crystal structures of JNK3 in complex with three different classes of inhibitors. These structures provide a clear picture of the interactions that each class of compound made with the kinase. Knowledge of the atomic interactions involved in these diverse binding modes provides a platform for structure-guided modification of these compounds, or the de novo design of novel inhibitors that could satisfy the need for potency and selectivity.
+The line below this paragraph, {{ABSTRACT_PUBMED_12954329}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_12954329}}
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 [[Category: Map kinase]]
 [[Category: Selectivity]]
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